纤维
生物物理学
化学
淀粉样纤维
硫黄素
蛋白质聚集
流变学
淀粉样蛋白(真菌学)
结晶学
材料科学
生物化学
淀粉样β
生物
复合材料
无机化学
阿尔茨海默病
病理
疾病
医学
作者
Ting Li,Li Wang,Xinxia Zhang,Han Geng,Wei Xue,Zhengxing Chen
标识
DOI:10.1016/j.foodhyd.2020.106396
摘要
The assembly behavior of three selected legume proteins was monitored using thioflavin T (ThT) fluorescence intensity, atomic force microscopy (AFM) and dynamic light scattering (DLS) in this test. It was found that the cowpea protein (CoP) had the highest ability to form amyloid fibrils due to the higher ThT fluorescence intensity of CoP fibrils than chickpea protein (ChP) fibrils and lentil protein (LP) fibrils. These legume proteins were partially denatured during initial heating period, and then the elongation of fibrils was occurred with prolonged heating time. Correspondingly, the particle size of legume proteins decreased firstly, probably resulting from the degraded polypeptides and disrupted structure under the heat treatment and acid hydrolysis. Then the particle size of proteins increased with increasing heating time due to the reorganization of ordered structure. From the results of SDS-PAGE and AFM, vicilin fractions were more beneficial to the formation of fibrils, and the longer and flexible fibrils were observed in the vicilin enriched CoP fibrils, whereas the semiflexible fibrils and rigid fibrils were occurred in LP and ChP fibrils, respectively. In addition, the rheological properties of CoP fibrils were superior to ChP and LP fibrils, owing to the tight entanglement of the longer and flexible CoP fibrils. This work will strengthen the understanding of the formation mechanism of different legume proteins based fibrils and explore their potential application.
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